Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans

The recent availability of an incomplete genomic sequence from Acidithiobacillus ferrooxidans allowed us to continue and strengthen the demanding task of investigating the proteome and its functional implications in this extremophilic microorganism. The proteins of At. ferrooxidans were separated by...

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Authors: JEREZ-GUEVARA, CARLOS, GUILIANI, NICOLAS, VERA, M.
Format: article
Status:Published version
Publication Date:2003
Country:Chile
Language:English
OAI Identifier:oai:repositorio.anid.cl:10533/197291
Online Access:https://hdl.handle.net/10533/197291
Access Level:Open access
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spelling VERA, M.GUILIANI, NICOLASJEREZ-GUEVARA, CARLOS200310.1016/S0304-386X(03)00148-8https://hdl.handle.net/10533/197291http://purl.org/coar/access_right/c_abf2Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans132125NLDAMSTERDAMJEREZ-GUEVARA, CARLOSGUILIANI, NICOLASVERA, M.2017-04-27T18:51:07Z2022-07-07T02:20:34Z2017-04-27T18:51:07Z2022-07-07T02:20:34Z2003The recent availability of an incomplete genomic sequence from Acidithiobacillus ferrooxidans allowed us to continue and strengthen the demanding task of investigating the proteome and its functional implications in this extremophilic microorganism. The proteins of At. ferrooxidans were separated by two-dimensional polyacrylamide gel electrophoresis and their levels of synthesis and the microsequencing of their N-terminal end amino acids were determined. To link the 2D gel spots of interest with the genes that encodes them, we studied the global changes in gene expression of At. ferrooxidans when the bacterium was confronted with phosphate starvation. By comparing the amino acid sequences of the proteins whose synthesis was induced or repressed under these conditions, with the available At. ferrooxidans genomic database, we found several putative genes whose expression may be related to phosphate starvation. Analysis of the genome DNA sequences upstream and downstream of these genes showed us details of the structure of putative operons present in At. ferrooxidans, strongly suggesting the existence of a Pho regulon containing the putative genes phoB, phoR, pstS, pstC,pstA, pYtB, phoU, ppx and ppk. Some differences were seen in the organization of the genes in the possible Pho regulon of At. ferrooxidans when compared with the Pho operons from other microorganisms. This was specially evident in the organization of the genes involved in polyphosphate metabolism (ppk and ppx). Regulation of phosphate metabolism is of particular relevance when At, ferrooxidans grows in the presence of arsenopyrites, which release arsenate, a structural analog of phosphate. Structural comparison between the specific phosphate-binding protein PstS from Escherichia coli and the corresponding At. ferrooxidans homolog showed that both proteins are highly conserved, including the phosphate/arsenate binding site, which shares seven of the eight amino acid residues necessary for the hydrogen bonding to the four oxygens of phosphate. (C) 2003 Elsevier B.V. All rights reserved.032FONDEF002FONDEF710D99I1026D99I1026virtual::39248-1WOS:000186357900016WOS:0001863579000160304-386Xhttps://hdl.handle.net/10533/197291ELSEVIER SCIENCE BVinstname: Conicytreponame: Repositorio Digital RI2.0instname: Conicytreponame: Repositorio Digital RI2.010.1016/S0304-386X(03)00148-8info:eu-repo/grantAgreement/Fondef/D99I1026info:eu-repo/semantics/dataset/hdl.handle.net/10533/93477https://doi.org/10.1016/S0304-386X(03)00148-8info:eu-repo/semantics/openAccessProteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidansHYDROMETALLURGYHydrometallurgyArticuloinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionengArticulohttps://hdl.handle.net/10533/197291FONDEFhttp://purl.org/coar/resource_type/c_2df8fbb1265ac432-2df3-41b6-bda1-0c095ec4262cvirtual::39248-1265ac432-2df3-41b6-bda1-0c095ec4262cvirtual::39248-110533/197291oai:repositorio.anid.cl:10533/1972912023-07-24 15:58:01.612https://repositorio.anid.clRepositorio ANIDaletelier@anid.cl
dc.title.none.fl_str_mv Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans
dc.title.journal.none.fl_str_mv HYDROMETALLURGY
dc.title.journalabbreviation.none.fl_str_mv Hydrometallurgy
title Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans
spellingShingle Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans
JEREZ-GUEVARA, CARLOS
title_short Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans
title_full Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans
title_fullStr Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans
title_full_unstemmed Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans
title_sort Proteomic and genomic analysis of the phosphate starvation response of acidithiobacillus ferrooxidans
dc.creator.none.fl_str_mv JEREZ-GUEVARA, CARLOS
GUILIANI, NICOLAS
VERA, M.
author JEREZ-GUEVARA, CARLOS
author_facet JEREZ-GUEVARA, CARLOS
GUILIANI, NICOLAS
VERA, M.
author_role author
author2 GUILIANI, NICOLAS
VERA, M.
author2_role author
author
description The recent availability of an incomplete genomic sequence from Acidithiobacillus ferrooxidans allowed us to continue and strengthen the demanding task of investigating the proteome and its functional implications in this extremophilic microorganism. The proteins of At. ferrooxidans were separated by two-dimensional polyacrylamide gel electrophoresis and their levels of synthesis and the microsequencing of their N-terminal end amino acids were determined. To link the 2D gel spots of interest with the genes that encodes them, we studied the global changes in gene expression of At. ferrooxidans when the bacterium was confronted with phosphate starvation. By comparing the amino acid sequences of the proteins whose synthesis was induced or repressed under these conditions, with the available At. ferrooxidans genomic database, we found several putative genes whose expression may be related to phosphate starvation. Analysis of the genome DNA sequences upstream and downstream of these genes showed us details of the structure of putative operons present in At. ferrooxidans, strongly suggesting the existence of a Pho regulon containing the putative genes phoB, phoR, pstS, pstC,pstA, pYtB, phoU, ppx and ppk. Some differences were seen in the organization of the genes in the possible Pho regulon of At. ferrooxidans when compared with the Pho operons from other microorganisms. This was specially evident in the organization of the genes involved in polyphosphate metabolism (ppk and ppx). Regulation of phosphate metabolism is of particular relevance when At, ferrooxidans grows in the presence of arsenopyrites, which release arsenate, a structural analog of phosphate. Structural comparison between the specific phosphate-binding protein PstS from Escherichia coli and the corresponding At. ferrooxidans homolog showed that both proteins are highly conserved, including the phosphate/arsenate binding site, which shares seven of the eight amino acid residues necessary for the hydrogen bonding to the four oxygens of phosphate. (C) 2003 Elsevier B.V. All rights reserved.
publishDate 2003
dc.date.issued.none.fl_str_mv 2003
dc.date.accessioned.none.fl_str_mv 2017-04-27T18:51:07Z
2022-07-07T02:20:34Z
dc.date.available.none.fl_str_mv 2017-04-27T18:51:07Z
2022-07-07T02:20:34Z
dc.type.none.fl_str_mv Articulo
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format article
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dc.identifier.folio.none.fl_str_mv D99I1026
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dc.identifier.issn.none.fl_str_mv 0304-386X
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/10533/197291
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reponame: Repositorio Digital RI2.0
dc.relation.doi.none.fl_str_mv 10.1016/S0304-386X(03)00148-8
dc.relation.projectid.none.fl_str_mv info:eu-repo/grantAgreement/Fondef/D99I1026
dc.relation.set.none.fl_str_mv info:eu-repo/semantics/dataset/hdl.handle.net/10533/93477
dc.relation.uri.none.fl_str_mv https://doi.org/10.1016/S0304-386X(03)00148-8
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dc.coverage.spatial.none.fl_str_mv AMSTERDAM
dc.publisher.none.fl_str_mv ELSEVIER SCIENCE BV
publisher.none.fl_str_mv ELSEVIER SCIENCE BV
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